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GrainGenes Reference Report: PNA-88-4114

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Reference
PNA-88-4114
Title
Primary structure of a cerulenin-binding beta ketoacyl-acyl carrier protein synthase from barley chloroplasts
Journal
Proceedings of the National Academy of Sciences, USA
Year
1991
Volume
88
Pages
4114-4118
Author
Siggaard-Andersen M
Kauppinen S
von Wettstein-Knowles P
Von-Wettstein-Knowles P
Abstract
The radioactively labeled .beta.-ketoacyl thioester synthase inhibitor [3H]cerulenin was used to tag three dimeric barley chloroplast proteins (.alpha..alpha., .alpha..beta., and .beta..beta.) from the stromal fraction. Oligonucleotides corresponding to amino acid sequences obtained from the purified proteins were used to generate with the polymerase chain reaction a probe for cDNAs encoding the .beta. subunit. cDNA sequencing revealed an open reading frame for 462 residues comprising the mature protein and a 35-amino acid transit peptide. The deduced amino acid sequence of the mature protein is homologous to the .beta.-ketoacyl [acyl carrier protein] (ACP) synthase I [3-oxoacyl- ACP synthase; acyl-ACP: malonyl-ACP C-acyltransferase (decarboxylating), EC 2.3.1.41] of Escherichia coli. Under analogous experimental conditions [3H]cerulenin tagged a single dimeric protein from spinach chloroplasts.
Probe
pSKc10
Keyword
Amino acid sequence
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